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. 2021 Feb 4;12:796. doi: 10.1038/s41467-021-21005-w

Fig. 7. X-ray crystal structures of T. thermophilus RNAP with ribo- and deoxyribonucloside substrates.

Fig. 7

Crystallographically observed binding poses of CMPCPP (a, b), 2′dCTP (c), and 3′dCTP (d) in the active site of T. thermophilus RNAP. Magenta numbers are interatomic distances in Å. Panels a and b were prepared using PDB ID 4Q4Z18. Pre-catalytic complexes in c and d were trapped due to the low reactivity of deoxyribonucleoside substrates and the slow catalysis by RNAP in crystallo52. Source data are provided as a Source Data file.